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Protein

Methyl-accepting chemotaxis protein I

Gene

tsr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids.
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.

GO - Molecular functioni

  • protein histidine kinase binding Source: EcoCyc
  • transmembrane signaling receptor activity Source: EcoCyc

GO - Biological processi

  • cell motility Source: CACAO
  • chemotaxis Source: CACAO
  • response to amino acid Source: EcoCyc
  • signal transduction Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

BioCyciEcoCyc:TSR-MONOMER.
ECOL316407:JW4318-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-accepting chemotaxis protein I
Short name:
MCP-I
Alternative name(s):
Serine chemoreceptor protein
Gene namesi
Name:tsr
Synonyms:cheD
Ordered Locus Names:b4355, JW4318
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11034. tsr.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 3024HelicalSequence analysisAdd
BLAST
Topological domaini31 – 190160PeriplasmicSequence analysisAdd
BLAST
Transmembranei191 – 21020HelicalSequence analysisAdd
BLAST
Topological domaini211 – 551341CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Methyl-accepting chemotaxis protein IPRO_0000110537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei297 – 2971Glutamate methyl ester (Gln)2 Publications
Modified residuei304 – 3041Glutamate methyl ester (Glu)2 Publications
Modified residuei311 – 3111Glutamate methyl ester (Gln)2 Publications
Modified residuei493 – 4931Glutamate methyl ester (Glu)2 Publications
Modified residuei502 – 5021Glutamate methyl ester (Glu)1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP02942.
PRIDEiP02942.

Interactioni

GO - Molecular functioni

  • protein histidine kinase binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261744. 200 interactions.
DIPiDIP-11046N.
IntActiP02942. 4 interactions.
MINTiMINT-1306492.
STRINGi511145.b4355.

Structurei

Secondary structure

1
551
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 7854Combined sources
Helixi87 – 11024Combined sources
Helixi119 – 14426Combined sources
Helixi148 – 1536Combined sources
Helixi156 – 18631Combined sources
Helixi296 – 32833Combined sources
Helixi332 – 36029Combined sources
Helixi362 – 38827Combined sources
Helixi390 – 3923Combined sources
Helixi393 – 43846Combined sources
Helixi441 – 4488Combined sources
Turni449 – 4513Combined sources
Helixi452 – 51564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QU7X-ray2.60A/B294-520[»]
2D4UX-ray1.95A/B25-190[»]
3ATPX-ray2.50A/B25-190[»]
3ZX6X-ray2.65A/B264-551[»]
DisProtiDP00300.
ProteinModelPortaliP02942.
SMRiP02942. Positions 39-189, 217-520.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02942.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 26853HAMPPROSITE-ProRule annotationAdd
BLAST
Domaini273 – 502230Methyl-accepting transducerPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 7310The 3 Arg may form a positively charged pocket, which binds the alpha-carboxyl group of the attractant AA

Sequence similaritiesi

Contains 1 HAMP domain.PROSITE-ProRule annotation
Contains 1 methyl-accepting transducer domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000148074.
InParanoidiP02942.
KOiK05874.
OMAiNALKHDK.
OrthoDBiEOG6G4VQG.
PhylomeDBiP02942.

Family and domain databases

Gene3Di1.20.120.30. 1 hit.
InterProiIPR004090. Chemotax_Me-accpt_rcpt.
IPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
IPR004091. Chemotax_Me-accpt_rcpt_Me-site.
IPR003660. HAMP_dom.
IPR004089. MCPsignal_dom.
[Graphical view]
PfamiPF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
PF02203. TarH. 1 hit.
[Graphical view]
PRINTSiPR00260. CHEMTRNSDUCR.
SMARTiSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
SM00319. TarH. 1 hit.
[Graphical view]
SUPFAMiSSF47170. SSF47170. 1 hit.
PROSITEiPS00538. CHEMOTAXIS_TRANSDUC_1. 1 hit.
PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKRIKIVTS LLLVLAVFGL LQLTSGGLFF NALKNDKENF TVLQTIRQQQ
60 70 80 90 100
STLNGSWVAL LQTRNTLNRA GIRYMMDQNN IGSGSTVAEL MESASISLKQ
110 120 130 140 150
AEKNWADYEA LPRDPRQSTA AAAEIKRNYD IYHNALAELI QLLGAGKINE
160 170 180 190 200
FFDQPTQGYQ DGFEKQYVAY MEQNDRLHDI AVSDNNASYS QAMWILVGVM
210 220 230 240 250
IVVLAVIFAV WFGIKASLVA PMNRLIDSIR HIAGGDLVKP IEVDGSNEMG
260 270 280 290 300
QLAESLRHMQ GELMRTVGDV RNGANAIYSG ASEIATGNND LSSRTEQQAA
310 320 330 340 350
SLEETAASME QLTATVKQNA ENARQASHLA LSASETAQRG GKVVDNVVQT
360 370 380 390 400
MRDISTSSQK IADIISVIDG IAFQTNILAL NAAVEAARAG EQGRGFAVVA
410 420 430 440 450
GEVRNLAQRS AQAAREIKSL IEDSVGKVDV GSTLVESAGE TMAEIVSAVT
460 470 480 490 500
RVTDIMGEIA SASDEQSRGI DQVGLAVAEM DRVTQQNAAL VEESAAAAAA
510 520 530 540 550
LEEQASRLTE AVAVFRIQQQ QRETSAVVKT VTPAAPRKMA VADSEENWET

F
Length:551
Mass (Da):59,443
Last modified:July 1, 1993 - v2
Checksum:iE8DB026029989B0F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00373 Genomic DNA. Translation: CAA23676.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97252.1.
U00096 Genomic DNA. Translation: AAC77311.1.
AP009048 Genomic DNA. Translation: BAE78345.1.
S56952 Genomic DNA. Translation: AAB25802.1.
PIRiE65250. QRECS.
RefSeqiNP_418775.1. NC_000913.3.
WP_000919536.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77311; AAC77311; b4355.
BAE78345; BAE78345; BAE78345.
GeneIDi948884.
KEGGiecj:JW4318.
eco:b4355.
PATRICi32124316. VBIEscCol129921_4501.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00373 Genomic DNA. Translation: CAA23676.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97252.1.
U00096 Genomic DNA. Translation: AAC77311.1.
AP009048 Genomic DNA. Translation: BAE78345.1.
S56952 Genomic DNA. Translation: AAB25802.1.
PIRiE65250. QRECS.
RefSeqiNP_418775.1. NC_000913.3.
WP_000919536.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QU7X-ray2.60A/B294-520[»]
2D4UX-ray1.95A/B25-190[»]
3ATPX-ray2.50A/B25-190[»]
3ZX6X-ray2.65A/B264-551[»]
DisProtiDP00300.
ProteinModelPortaliP02942.
SMRiP02942. Positions 39-189, 217-520.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261744. 200 interactions.
DIPiDIP-11046N.
IntActiP02942. 4 interactions.
MINTiMINT-1306492.
STRINGi511145.b4355.

Proteomic databases

PaxDbiP02942.
PRIDEiP02942.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77311; AAC77311; b4355.
BAE78345; BAE78345; BAE78345.
GeneIDi948884.
KEGGiecj:JW4318.
eco:b4355.
PATRICi32124316. VBIEscCol129921_4501.

Organism-specific databases

EchoBASEiEB1027.
EcoGeneiEG11034. tsr.

Phylogenomic databases

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000148074.
InParanoidiP02942.
KOiK05874.
OMAiNALKHDK.
OrthoDBiEOG6G4VQG.
PhylomeDBiP02942.

Enzyme and pathway databases

BioCyciEcoCyc:TSR-MONOMER.
ECOL316407:JW4318-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02942.
PROiP02942.

Family and domain databases

Gene3Di1.20.120.30. 1 hit.
InterProiIPR004090. Chemotax_Me-accpt_rcpt.
IPR003122. Chemotax_Me-accpt_rcpt_lig-bd.
IPR004091. Chemotax_Me-accpt_rcpt_Me-site.
IPR003660. HAMP_dom.
IPR004089. MCPsignal_dom.
[Graphical view]
PfamiPF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
PF02203. TarH. 1 hit.
[Graphical view]
PRINTSiPR00260. CHEMTRNSDUCR.
SMARTiSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
SM00319. TarH. 1 hit.
[Graphical view]
SUPFAMiSSF47170. SSF47170. 1 hit.
PROSITEiPS00538. CHEMOTAXIS_TRANSDUC_1. 1 hit.
PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the serine chemoreceptor in Escherichia coli."
    Boyd A., Kendall K., Simon M.I.
    Nature 301:623-626(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The Escherichia coli C homoprotocatechuate degradative operon: hpc gene order, direction of transcription and control of expression."
    Roper D.I., Fawcett T., Cooper R.A.
    Mol. Gen. Genet. 237:241-250(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
    Strain: C.
  6. "The methyl-accepting chemotaxis proteins of Escherichia coli. Identification of the multiple methylation sites on methyl-accepting chemotaxis protein I."
    Kehry M.R., Dahlquist F.W.
    J. Biol. Chem. 257:10378-10386(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 295-317 AND 483-507, METHYLATION.
  7. "Sites of deamidation and methylation in Tsr, a bacterial chemotaxis sensory transducer."
    Rice M.S., Dahlquist F.W.
    J. Biol. Chem. 266:9746-9753(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT GLN-297; GLU-304; GLN-311; GLU-493 AND GLU-502, DEAMIDATION AT GLN-297 AND GLN-311.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  10. "Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli."
    Li G., Young K.D.
    Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  11. "Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor."
    Kim K.K., Yokota H., Kim S.-H.
    Nature 400:787-792(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 294-520.

Entry informationi

Entry nameiMCP1_ECOLI
AccessioniPrimary (citable) accession number: P02942
Secondary accession number(s): P76817, Q2M5W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1993
Last modified: January 20, 2016
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.